The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
A serine/threonine kinase gene defective in Peutz–Jeghers syndrome
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Lessons from hereditary colorectal cancer
Kinzler, K. W., & Vogelstein, B. (1996) · Cell · doi:10.1016/s0092-8674(00)81333-1 · Cited by 4,919
Germline mutations in the p16INK4a binding domain of CDK4 in familial melanoma
Zuo, L., Weger, J., Yang, Q., Goldstein, A. M., Tucker, M. A., Walker, G. J., Hayward, N., & Dracopoli, N. C. (1996) · Nature Genetics · doi:10.1038/ng0196-97 · Cited by 818
Cited by
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849
A census of human cancer genes
Futreal, P. A., Coin, L., Marshall, M., Down, T., Hubbard, T., Wooster, R., Rahman, N., & Stratton, M. R. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1299 · Cited by 3,184
Self-citationRas, PI(3)K and mTOR signalling controls tumour cell growth
Shaw, R. J., & Cantley, L. C. (2006) · Nature · doi:10.1038/nature04869 · Cited by 2,019
The LKB1-AMPK pathway: metabolism and growth control in tumour suppression
Shackelford, D. B., & Shaw, R. J. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2676 · Cited by 1,943
LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., Schlattner, U., Wallimann, T., Carlson, M., & Carling, D. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.031 · Cited by 1,650
AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function
Hardie, D. G. (2011) · Genes & Development · doi:10.1101/gad.17420111 · Cited by 1,638
LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR‐1
Lizcano, J. M., Göransson, O., Toth, R., Deak, M., Morrice, N. A., Boudeau, J., Hawley, S. A., Udd, L., Mäkelä, T. P., Hardie, D. G., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600110 · Cited by 1,381
The AMP‐Activated Protein Kinase: Fuel Gauge of the Mammalian Cell?
Hardie, D. G., & Carling, D. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00259.x · Cited by 1,317
Metabolic Regulation of T Lymphocytes
MacIver, N. J., Michalek, R. D., & Rathmell, J. C. (2013) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032712-095956 · Cited by 1,244
Autophagy in malignant transformation and cancer progression
Galluzzi, L., Pietrocola, F., Bravo‐San Pedro, J. M., Amaravadi, R. K., Baehrecke, E. H., Cecconi, F., Codogno, P., Debnath, J., Gewirtz, D. A., Karantza, V., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201490784 · Cited by 1,182
Metformin is an AMP kinase-dependent growth inhibitor for breast cancer cells
Zakikhani, M., Dowling, R., Fantus, I. G., Sonenberg, N., & Pollak, M. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1500 · Cited by 1,048
Dowling, R. J. O., Zakikhani, M., Fantus, I. G., Pollak, M., & Sonenberg, N. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2310 · Cited by 933
AMP-Activated Protein Kinase – Development of the Energy Sensor Concept
Hardie, D. G., Hawley, S. A., & Scott, J. W. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.108944 · Cited by 813
The role of ubiquitination in tumorigenesis and targeted drug discovery
Deng, L., Meng, T., Chen, L., Wei, W., & Wang, P. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0107-0 · Cited by 744
LKB1 and AMP-activated protein kinase control of mTOR signalling and growth
Shaw, R. J. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01972.x · Cited by 644
Shackelford, D. B., Abt, E., Gerken, L., Vasquez, D. S., Seki, A., Leblanc, M., Wei, L., Fishbein, M. C., Czernin, J., Mischel, P. S., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2012.12.008 · Cited by 585
Metabolic switching and fuel choice during T‐cell differentiation and memory development
van der Windt, G. J. W., & Pearce, E. L. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01150.x · Cited by 563
Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
Hahn-Windgassen, A., Nogueira, V., Chen, C.-C., Skeen, J. E., Sonenberg, N., & Hay, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502876200 · Cited by 539
Lkb1 regulates cell cycle and energy metabolism in haematopoietic stem cells
Nakada, D., Saunders, T. L., & Morrison, S. J. (2010) · Nature · doi:10.1038/nature09571 · Cited by 524
BRCA2 germline mutations in familial pancreatic carcinoma
Hahn, S. A., Greenhalf, B., Ellis, I., Sina-Frey, M., Rieder, H., Korte, B., Gerdes, B., Kress, R., Ziegler, A., Raeburn, J. A., et al. (2003) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/95.3.214 · Cited by 480
Protean PTEN: Form and Function
Waite, K. A., & Eng, C. (2002) · The American Journal of Human Genetics · doi:10.1086/340026 · Cited by 457
Amino acids and mTORC1: from lysosomes to disease
Efeyan, A., Zoncu, R., & Sabatini, D. M. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.05.007 · Cited by 436
“Orlova KA, et al. STRADalpha deficiency results in aberrant mTORC1 signaling during corticogenesis in humans and mice.”
Hereditary breast and ovarian cancer: new genes in confined pathways
Nielsen, F. C., van Overeem Hansen, T., & Sørensen, C. S. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.72 · Cited by 367
Loss of the Tumor Suppressor LKB1 Promotes Metabolic Reprogramming of Cancer Cells via HIF-1α
Faubert, B., Vincent, E. E., Griss, T., Samborska, B., Izreig, S., Svensson, R. U., Mamer, O. A., Avizonis, D., Shackelford, D. B., Shaw, R. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312570111 · Cited by 278
Xie, Z., Dong, Y., Scholz, R., Neumann, D., & Zou, M.-H. (2008) · Circulation · doi:10.1161/circulationaha.107.744490 · Cited by 273
Rapamycin: an anti-cancer immunosuppressant?
Law, B. K. (2005) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2004.09.009 · Cited by 252
The liver kinase B1 is a central regulator of T cell development, activation, and metabolism
MacIver, N. J., Blagih, J., Saucillo, D. C., Tonelli, L., Griss, T., Rathmell, J. C., & Jones, R. G. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100367 · Cited by 235
Zhou, L., Deepa, S. S., Etzler, J. C., Ryu, J., Mao, X., Fang, Q., Liu, D. D., Torres, J. M., Jia, W., Lechleiter, J. D., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028357 · Cited by 212
Koh, H.-J., Arnolds, D. E., Fujii, N., Tran, T. T., Rogers, M. J., Jessen, N., Li, Y., Liew, C. W., Ho, R. C., Hirshman, M. F., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00979-06 · Cited by 202
New Roles for the LKB1-NUAK Pathway in Controlling Myosin Phosphatase Complexes and Cell Adhesion
Zagórska, A., Deak, M., Campbell, D. G., Banerjee, S., Hirano, M., Aizawa, S., Prescott, A. R., & Alessi, D. R. (2010) · Science Signaling · doi:10.1126/scisignal.2000616 · Cited by 193
ABINs: A20 binding inhibitors of NF-κB and apoptosis signaling
Verstrepen, L., Carpentier, I., Verhelst, K., & Beyaert, R. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.02.009 · Cited by 180
Morton, J. P., Jamieson, N. B., Karim, S. A., Athineos, D., Ridgway, R. A., Nixon, C., McKay, C. J., Carter, R., Brunton, V. G., Frame, M. C., et al. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.04.055 · Cited by 169
The AMPK-Related Kinases SIK1 and SIK3 Mediate Key Tumor-Suppressive Effects of LKB1 in NSCLC
Hollstein, P. E., Eichner, L. J., Brun, S. N., Kamireddy, A., Svensson, R. U., Vera, L. I., Ross, D. S., Rymoff, T. J., Hutchins, A., Galvez, H. M., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-1261 · Cited by 168
Cardiac-specific deletion of LKB1 leads to hypertrophy and dysfunction
Ikeda, Y., Sato, K., Pimentel, D. R., Sam, F., Shaw, R. J., Dyck, J. R. B., & Walsh, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057273 · Cited by 164
Nutrient-sensing pathways and metabolic regulation in stem cells
Ochocki, J. D., & Simon, M. C. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201303110 · Cited by 140
Hruban, R. H., Petersen, G. M., Goggins, M., Tersmette, A. C., Offerhaus, G. J. A., Falatko, F., Yeo, C. J., & Kern, S. E. (1999) · Annals of Oncology · doi:10.1093/annonc/10.suppl_4.s69 · Cited by 134
Calles, A., Sholl, L. M., Rodig, S. J., Pelton, A. K., Hornick, J. L., Butaney, M., Lydon, C., Dahlberg, S. E., Oxnard, G. R., Jackman, D. M., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3112 · Cited by 115
An LKB1–SIK Axis Suppresses Lung Tumor Growth and Controls Differentiation
Murray, C. W., Brady, J. J., Tsai, M. K., Li, C., Winters, I. P., Tang, R., Andrejka, L., Ma, R. K., Kunder, C. A., Chu, P., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-1237 · Cited by 111
Targeting LKB1 in Cancer – Exposing and Exploiting Vulnerabilities
Momcilovic, M., & Shackelford, D. B. (2015) · British Journal of Cancer · doi:10.1038/bjc.2015.261 · Cited by 97
LKB1 is essential for the proliferation of T‐cell progenitors and mature peripheral T cells
Tamás, P., Macintyre, A., Finlay, D., Clarke, R., Feijoo‐Carnero, C., Ashworth, A., & Cantrell, D. (2010) · European Journal of Immunology · doi:10.1002/eji.200939677 · Cited by 94
International registries of families at high risk of pancreatic cancer
Greenhalf, W., Malats, N., Nilsson, M., Bartsch, D., & Neoptolemos, J. (2008) · Pancreatology · doi:10.1159/000159843 · Cited by 85
AMP-activated protein kinase conducts the ischemic stress response orchestra
Young, L. H. (2008) · Circulation · doi:10.1161/circulationaha.107.713115 · Cited by 82
Wan, S., Meyer, A., Weiler, S. M. E., Rupp, C., Tóth, M., Sticht, C., Singer, S., Thomann, S., Roessler, S., Schorpp‐Kistner, M., et al. (2018) · Hepatology · doi:10.1002/hep.29669 · Cited by 79
Controlling the master—upstream regulation of the tumor suppressor LKB1
Kullmann, L., & Krahn, M. P. (2018) · Oncogene · doi:10.1038/s41388-018-0145-z · Cited by 75
GSK-3β Directly Phosphorylates and Activates MARK2/PAR-1
Kosuga, S., Tashiro, E., Kajioka, T., Ueki, M., Shimizu, Y., & Imoto, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507941200 · Cited by 57
Yamada, T., Amann, J. M., Tanimoto, A., Taniguchi, H., Shukuya, T., Timmers, C., Yano, S., Shilo, K., & Carbone, D. P. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0146 · Cited by 44
Skeletal muscle dysfunction in muscle-specific LKB1 knockout mice.
Thomson, D. M., Hancock, C. R., Evanson, B. G., Kenney, S. G., Malan, B. B., Mongillo, A. D., Brown, J. D., Hepworth, S., Fillmore, N., Parcell, A. C., et al. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01293.2009 · Cited by 45
Convergence of IPMK and LKB1-AMPK Signaling Pathways on Metformin Action
Bang, S., Chen, Y., Ahima, R. S., & Kim, S. F. (2014) · Molecular Endocrinology · doi:10.1210/me.2014-1134 · Cited by 45
PKA Activates AMPK Through LKB1 Signaling in Follicular Thyroid Cancer
Kari, S., Vasko, V. V., Priya, S., & Kirschner, L. S. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00769 · Cited by 34
Nallar, S. C., Kalakonda, S., Lindner, D. J., Lorenz, R. R., Lamarre, E., Weihua, X., & Kalvakolanu, D. V. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.440610 · Cited by 29
No evidence for germline mutations of the LKB1/STK11 gene in familial pancreatic carcinoma
Grützmann, R., McFaul, C., Bartsch, D. K., Sina-Frey, M., Rieder, H., Koch, R., McCarthy, E., Greenhalf, W., Neoptolemos, J. P., Saeger, H. D., et al. (2004) · Cancer Letters · doi:10.1016/j.canlet.2004.06.012 · Cited by 23
(2007) · PubMed · Cited by 15
Metadata
- Authors
- Hemminki, A., Markie, D., Tomlinson, I., Avizienyte, E., Roth, S., Loukola, A., Bignell, G., Warren, W., Aminoff, M., Höglund, P., Järvinen, H., Kristo, P., Pelin, K., Ridanpää, M., Salovaara, R., Toro, T., Bodmer, W., Olschwang, S., Olsen, A. S., Stratton, M. R., de la Chapelle, A., & Aaltonen, L. A.
- Venue
- Nature
- Published
- 1998-01
- Volume
- 391
- Issue
- 6663
- Pages
- 184-187
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1619256199
- Cited by
- 1,656
- References
- 2
- FWCI
- 42.23
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.